| Download | - View accepted manuscript: Topological study of mechanistic diversity in conjugated fatty acid biosynthesis (PDF, 606 KiB)
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| DOI | Resolve DOI: https://doi.org/10.1002/anie.201202080 |
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| Author | Search for: Bhar, Palash; Search for: Reed, Darwin W.1; Search for: Covello, Patrick S.1; Search for: Buist, Peter H. |
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| Affiliation | - National Research Council of Canada. NRC Plant Biotechnology Institute
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| Format | Text, Article |
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| Subject | C−H activation; desaturases; enzyme mechanisms; kinetic isotope effects; conformation analysis |
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| Abstract | Variations on an oxidative theme: The precision with which FAD2-type desaturases carry out C−H activation reactions on flexible lipidic substrates is astonishing. The conformational space available within the active site of these enzymes has been explored using deuterium-labeled substrates, and evidence for a novel quasi-eclipsed conformer has been uncovered. The scheme shows some prototypical substrate conformations. |
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| Publication date | 2012-05-23 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRCC 54667 |
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| NPARC number | 21186090 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | fa710324-f63e-4cc1-b7b6-f0391d33fdde |
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| Record created | 2013-01-09 |
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| Record modified | 2020-04-21 |
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